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(Received for publication, March 21, 1996, and in revised form, June 4, 1996)
,
From the Department of Dermatology, University of Kiel, D-24105
Kiel, Germany and the The stratum corneum chymotryptic enzyme (SCCE)
has been previously purified from human stratum corneum and resembles a
chymotryptic serine endopeptidase involved in physiological detachment
of corneocytes from human stratum corneum. From human stratum corneum
two inhibitory activities of SCCE could be extracted. These were due to
serine protease inhibitors already known to be present in human
epidermis, antileukoprotease (secretory leukocyte protease inhibitor)
and elafin (skin-derived antileukoprotease). The Inhibition of SCCE by
antileukoprotease shows a hyperbolic, mixed type inhibition with an
equilibrium dissociation constant of 63 nM.
Antileukoprotease also inhibits detachment of corneocytes from human
plantar callus in vitro almost completely (>96%). In
addition, elafin was shown to be a weak inhibitor for SCCE activity,
and elafin significantly reduces the shedding of corneocytes. Thus,
antileukoprotease, which is known to be produced by human
keratinocytes, is likely to be the major physiological inhibitor of
SCCE in the epidermis. It seems to be involved in the regulation of
desquamation under physiological and pathophysiological conditions.
Department of Rheumatology,
University Hospital of Zürich, CH-8091 Zurich, Switzerland
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